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Database: UniProt
Entry: A0A2K6EXB5_PROCO
LinkDB: A0A2K6EXB5_PROCO
Original site: A0A2K6EXB5_PROCO 
ID   A0A2K6EXB5_PROCO        Unreviewed;       863 AA.
AC   A0A2K6EXB5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=DNM3 {ECO:0000313|Ensembl:ENSPCOP00000006377.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000006377.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000006377.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR   RefSeq; XP_012513232.1; XM_012657778.1.
DR   AlphaFoldDB; A0A2K6EXB5; -.
DR   Ensembl; ENSPCOT00000016912.1; ENSPCOP00000006377.1; ENSPCOG00000014334.1.
DR   GeneID; 105821143; -.
DR   CTD; 26052; -.
DR   GeneTree; ENSGT00940000158056; -.
DR   OrthoDB; 1052588at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd08771; DLP_1; 1.
DR   CDD; cd01256; PH_dynamin; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF54; DYNAMIN-3; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT   DOMAIN          28..294
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          515..621
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          653..744
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          627..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..820
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..852
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97256 MW;  F571BC3AFDEA6D31 CRC64;
     MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVTSKAEY AEFLHSKGKK FTDFDEVRHE IEAETDRVTG MNKGISSIPI
     NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIREMI MQFITRENCL ILAVTPANTD
     LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YVGVVNRSQK
     DIDGKKDIKA AMLAERKFFL SHPAYRHIAD RMGTPHLQKV LNQQLTNHIR DTLPNFRNKL
     QGQLLSIEHE VEAYKNFKPE DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA
     KINRIFHERF PFEIVKMEFN EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL
     KGPSLKSVDL VIQELINTVK KCTKKLANFP RLCEETERIV ANHIREREGK TKDQVLLLID
     IQVSYINTNH EDFIGFANAQ QRSSQVHKKT TIGNQVIRKG WLTISNIGIM KGGSKGYWFV
     LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKSFMSSKH IFALFNTEQR NVYKDYRFLE
     LACDSQEDVD SWKASLLRAG VYPDKSLGNN KTENDENGQA ENFSMDPQLE RQVETIRNLV
     DSYMSIINKC IRDLIPKTIM HLMINNVKDF INSELLAQLY SSEDQNTLME ESAEQAQRRD
     EMLRMYQALK EALVIIGDIN TATVSTPAPP PVDDSWIQHS RRSPPPSPTT PRRPTLSAPL
     TRPTSGRGPA PAIPSPGPHS GAPPVPFRPG PLPPFPNSSD SFGAPPQVPS RPTRAPPSVP
     SRRPPPSPTR PTIIRPLESS LLD
//
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